(all-E)-15,15'-dihydro-β-β-carotene | 6895-64-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: (all-E)-15,15'-dihydro-β-β-carotene
• 英文别名: β,β-carotene；all-trans-15,15'-Dehydro-β-carotin；15,15'-Dehydro-β-carotin；1,3,3-trimethyl-2-[(1E,3E,5E,7E,11E,13E,15E,17E)-3,7,12,16-tetramethyl-18-(2,6,6-trimethylcyclohexen-1-yl)octadeca-1,3,5,7,11,13,15,17-octaenyl]cyclohexene
• CAS: 6895-64-3；128240-74-4
• 化学式: C₄₀H₅₈
• 分子量: 538.901
• InChiKey: MZFUCCXRKZISLZ-AYPYYXBOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  13.5
• 重原子数：
  40
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  0
• 氢给体数：
  0
• 氢受体数：
  0

反应信息

• 作为产物：
  描述：

  香叶醇 在 selenium(IV) oxide 、 sodium methylate 作用下， 以 甲醇 、 乙醇 、 水 为溶剂， 生成 (all-E)-15,15'-dihydro-β-β-carotene
  参考文献：
  名称：

  The Substrate Specificity ofβ,β-Carotene 15,15′-Monooxygenase

  摘要：

  The synthesis of several substrate analogues of the enzyme beta,beta -carotene 15,15'-monooxygenase is reported. The substrate specificity of enriched enzyme fractions isolated from chicken intestinal mucosa was investigated. Regarding substrate binding/cleavage, these experiments demonstrate that i) any deviation from the 'rod-like' beta,beta -carotene structure is not tolerated, ii) one 'natural', unsubstituted beta -ionone ring is required, iii) the position and presence of the Me groups attached to the polyene chain is significant. These results suggest a hydrophobic barrel-like substrate binding site in which the protein's amino acid residues through interaction with the Me groups, direct the central C=C bond in binding distance to the active site's metal-oxo center, supporting the unique regiospecificity of cleavage to retinal (provitamin A).

  DOI：

  10.1002/1522-2675(20010815)84:8<2301::aid-hlca2301>3.0.co;2-u

文献信息

• The Substrate Specificity ofβ,β-Carotene 15,15′-Monooxygenase
  作者：Gabriele M. Wirtz、Claus Bornemann、Alfred Giger、Robert K. Müller、Heinz Schneider、Götz Schlotterbeck、Gerhard Schiefer、Wolf-Dietrich Woggon

  DOI：10.1002/1522-2675(20010815)84:8<2301::aid-hlca2301>3.0.co;2-u

  日期：2001.8.15

  The synthesis of several substrate analogues of the enzyme beta,beta -carotene 15,15'-monooxygenase is reported. The substrate specificity of enriched enzyme fractions isolated from chicken intestinal mucosa was investigated. Regarding substrate binding/cleavage, these experiments demonstrate that i) any deviation from the 'rod-like' beta,beta -carotene structure is not tolerated, ii) one 'natural', unsubstituted beta -ionone ring is required, iii) the position and presence of the Me groups attached to the polyene chain is significant. These results suggest a hydrophobic barrel-like substrate binding site in which the protein's amino acid residues through interaction with the Me groups, direct the central C=C bond in binding distance to the active site's metal-oxo center, supporting the unique regiospecificity of cleavage to retinal (provitamin A).